Publication | Open Access
Mixing Aβ(1–40) and Aβ(1–42) peptides generates unique amyloid fibrils
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Citations
37
References
2020
Year
Protein AssemblyPeptide EngineeringMolecular BiologyRecent Structural StudiesPeptide ScienceCytoskeletonAnalytical UltracentrifugationProtein FoldingProtein MisfoldingMacromolecular AssembliesProtein FunctionBiochemistryMixed Fibrillar SpeciesDistinct MorphologiesStructural BiologyNeurodegenerative DiseasesNatural SciencesUnique Amyloid FibrilsProtein EngineeringMedicine
Recent structural studies show distinct morphologies for the fibrils of Aβ(1-42) and Aβ(1-40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1 : 1 mixed fibrillar species, which differs from both pure fibrils. It forms preferentially even when Aβ(1-42) : Aβ(1-40) peptides are mixed in a non-stoichiometric ratio.
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